1. Membrane-Active Peptides and the Clustering of Anionic Lipids
P. Wadhwani, R.F. Epand, N. Heidenreich, J. Bürck, A.S. Ulrich, R.M. Epand 
Biophysical Journal 
Volume 103, Issue 2, Pages (July 2012)
DOI: /j.bpj
Copyright © 2012 Biophysical Society Terms and Conditions

2. Figure 1
DSC of the lipid mixture POPE/TOCL (75:25) in the absence and presence of peptides at L/P = 20. Positive values correspond to heating, and negative values correspond to cooling. The first cycle of heating and cooling from 0°C to 25°C is in the lipid alone, followed by two cycles of heating and cooling in the presence of peptide. All scans were performed at a scan rate of 1°/min. (A) Clustering by AMPs. (B) Clustering by CPPs.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2012 Biophysical Society Terms and Conditions

3. Figure 2
CD spectra measured at 30°C of the investigated peptides in the presence of SUVs composed of POPE/TOCL (75:25) at an L/P molar ratio of 100. (A) CD spectra of the AMPs (gramicidin S, MSI-103, MSI-103-Arg, PGLa, PGLa-Arg, magainin 2, magainin 2-Arg, KIGAKI, and BP100). (B) CD spectra of the CPPs (MAP, MAP-Arg, penetratin, SAP, PEP1, transportan, HIV-TAT) and the fusion peptide (FP23).
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2012 Biophysical Society Terms and Conditions

4. Figure 3
Maximum temperature shift of the main transition obtained by DSC in the presence of peptide (Fig. 1, A and B, Table 2), with respect to the lipid mixture in the absence of peptide, Δλ, plotted as a function of the peptide's net positive charge. The short peptides BP100 and HIV-TAT fall out of line. The linear relationship holds for the AMPs (solid squares) as well as for the CPPs (open squares).
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2012 Biophysical Society Terms and Conditions